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Clinical and Diagnostic Laboratory Immunology, January 1998, p. 50-57, Vol. 5, No. 1
Cincinnati Veterans Affairs Medical
Center,1
Department of Internal
Medicine,
Received 29 May 1997/Returned for modification 31 July
1997/Accepted 2 October 1997
The major surface glycoprotein (MSG) of Pneumocystis
carinii f. sp. carinii consists of a heterogeneous
family of proteins that are encoded by approximately 100 unique genes.
A genomic expression library was screened with a panel of MSG-specific
monoclonal antibodies (MAbs) to identify conserved and rare epitopes.
All of the antibodies reacted with epitopes that are encoded within the
5' end of MSG. The results from the expression screening identified antibodies that recognize highly conserved, moderately conserved, and
rare epitopes. Four MAbs (MAbs RA-F1, RA-E7, RA-G10, and RB-E3) reacted
with a maltose binding protein-MSG-B fusion protein
(MBPMSG-B41-1065) by immunoblotting and
enzyme-linked immunosorbent assay. Three of the MAbs (MAbs RA-F1,
RA-G10, and RA-E7) reacted with the same continuous epitope that was
localized to amino acids 278 to 290 of MSG-B. Comparison of the
sequence of the RA-F1-, RA-G10-, and RA-E7-reactive epitope to the
deduced amino acid sequences of multiple MSGs demonstrated that it is
highly conserved. The reactivity of RB-E3 with MSG-B was shown to be
dependent on amino acids 184 to 192, which may comprise a portion of a
discontinuous epitope.
1071-412X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Expression, Structure, and Location of Epitopes of
the Major Surface Glycoprotein of Pneumocystis carinii f.
sp. carinii
*
Corresponding author. Mailing address: VA Medical
Center, 3200 Vine St., Cincinnati, OH 45220. Phone: (513) 861-3100, extension 4423. Fax: (513) 475-6415. E-mail: mjl19{at}juno.com.
Clinical and Diagnostic Laboratory Immunology, January 1998, p. 50-57, Vol. 5, No. 1
1071-412X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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